ID A0A1T5B798_9BACT Unreviewed; 332 AA.
AC A0A1T5B798;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=D-lactate dehydrogenase {ECO:0000313|EMBL:SKB43154.1};
GN ORFNames=SAMN05660293_00078 {ECO:0000313|EMBL:SKB43154.1};
OS Dyadobacter psychrophilus.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC Dyadobacter.
OX NCBI_TaxID=651661 {ECO:0000313|EMBL:SKB43154.1, ECO:0000313|Proteomes:UP000190897};
RN [1] {ECO:0000313|EMBL:SKB43154.1, ECO:0000313|Proteomes:UP000190897}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22270 {ECO:0000313|EMBL:SKB43154.1,
RC ECO:0000313|Proteomes:UP000190897};
RA Peterson S.W.;
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00005854,
CC ECO:0000256|RuleBase:RU003719}.
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DR EMBL; FUZA01000001; SKB43154.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T5B798; -.
DR STRING; 651661.SAMN05660293_00078; -.
DR OrthoDB; 1522997at2; -.
DR Proteomes; UP000190897; Unassembled WGS sequence.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR CDD; cd12183; LDH_like_2; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom.
DR InterPro; IPR029753; D-isomer_DH_CS.
DR InterPro; IPR029752; D-isomer_DH_CS1.
DR InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR43026; 2-HYDROXYACID DEHYDROGENASE HOMOLOG 1-RELATED; 1.
DR PANTHER; PTHR43026:SF1; 2-HYDROXYACID DEHYDROGENASE HOMOLOG 1-RELATED; 1.
DR Pfam; PF00389; 2-Hacid_dh; 1.
DR Pfam; PF02826; 2-Hacid_dh_C; 1.
DR SUPFAM; SSF52283; Formate/glycerate dehydrogenase catalytic domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00065; D_2_HYDROXYACID_DH_1; 1.
DR PROSITE; PS00670; D_2_HYDROXYACID_DH_2; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003719}.
FT DOMAIN 3..326
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 110..297
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 332 AA; 36908 MW; 6D0E3D794199FA40 CRC64;
MKILFFSAKP YDKQFFDLYN EDYGFEIEYL ETHLGPHIVN TVQDQQAVCV FVNDKVNAEV
ISILAKKGVK IIALRCAGFN NVDLDAARAH GIRVCRVPEY SPQAVAEHTV AMLLTLNRKT
HKAYNRVREQ DFSLNGLMGF NLYGKTVGVI GTGKIGGAFC RIMLGFGCKV KAYDLYPNKE
LESSGVVYTA LEDVLVSSDI ISLHCPLNED THYIINEKTI ATMRTGVALI NTSRGGLINT
ADIIEALKSK RVAYLGIDVY EQEEKLFFRD LSGSIIDDDV IQRLISFPNV LITAHQAFFT
QEALSEIAQI TLKSINDLAC GQKPENNSIV LV
//
